(6 nodes) Unfolded protein binding, and Heat shock protein 70, conserved site network (Mycobacterium gordonae)

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protein homology

Your Input:
	dnaJ	Molecular chaperone DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, [...] (383 aa)
	OBJ90234.1	Molecular chaperone Hsp70; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heat shock protein 70 family. (509 aa)
	groEL	Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (397 aa)
	dnaK	Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. (622 aa)
	htpG	Molecular chaperone HtpG; Molecular chaperone. Has ATPase activity. (648 aa)
	groEL-4	Molecular chaperone GroEL; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. (100 aa)

Your Current Organism:

Mycobacterium gordonae

NCBI taxonomy Id: 1778
Other names: ATCC 14470, CCUG 21801, CCUG 21811, CIP 104529, DSM 44160, JCM 6382, M. gordonae, NCTC 10267

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
OBJ90234.1	dnaJ	A9W97_13455	A9W97_11200	Molecular chaperone Hsp70; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heat shock protein 70 family.	Molecular chaperone DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, [...]	0.973
OBJ90234.1	dnaK	A9W97_13455	A9W97_18445	Molecular chaperone Hsp70; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heat shock protein 70 family.	Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.	0.909
OBJ90234.1	groEL	A9W97_13455	A9W97_14565	Molecular chaperone Hsp70; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heat shock protein 70 family.	Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.	0.928
OBJ90234.1	groEL-4	A9W97_13455	A9W97_30060	Molecular chaperone Hsp70; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heat shock protein 70 family.	Molecular chaperone GroEL; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.	0.869
OBJ90234.1	htpG	A9W97_13455	A9W97_22200	Molecular chaperone Hsp70; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heat shock protein 70 family.	Molecular chaperone HtpG; Molecular chaperone. Has ATPase activity.	0.997
dnaJ	OBJ90234.1	A9W97_11200	A9W97_13455	Molecular chaperone DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, [...]	Molecular chaperone Hsp70; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heat shock protein 70 family.	0.973
dnaJ	dnaK	A9W97_11200	A9W97_18445	Molecular chaperone DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, [...]	Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.	0.997
dnaJ	groEL	A9W97_11200	A9W97_14565	Molecular chaperone DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, [...]	Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.	0.943
dnaJ	groEL-4	A9W97_11200	A9W97_30060	Molecular chaperone DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, [...]	Molecular chaperone GroEL; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.	0.779
dnaJ	htpG	A9W97_11200	A9W97_22200	Molecular chaperone DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, [...]	Molecular chaperone HtpG; Molecular chaperone. Has ATPase activity.	0.994
dnaK	OBJ90234.1	A9W97_18445	A9W97_13455	Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.	Molecular chaperone Hsp70; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heat shock protein 70 family.	0.909
dnaK	dnaJ	A9W97_18445	A9W97_11200	Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.	Molecular chaperone DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, [...]	0.997
dnaK	groEL	A9W97_18445	A9W97_14565	Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.	Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.	0.982
dnaK	groEL-4	A9W97_18445	A9W97_30060	Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.	Molecular chaperone GroEL; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.	0.984
dnaK	htpG	A9W97_18445	A9W97_22200	Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.	Molecular chaperone HtpG; Molecular chaperone. Has ATPase activity.	0.999
groEL	OBJ90234.1	A9W97_14565	A9W97_13455	Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.	Molecular chaperone Hsp70; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heat shock protein 70 family.	0.928
groEL	dnaJ	A9W97_14565	A9W97_11200	Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.	Molecular chaperone DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, [...]	0.943
groEL	dnaK	A9W97_14565	A9W97_18445	Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.	Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.	0.982
groEL	groEL-4	A9W97_14565	A9W97_30060	Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.	Molecular chaperone GroEL; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.	0.999
groEL	htpG	A9W97_14565	A9W97_22200	Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.	Molecular chaperone HtpG; Molecular chaperone. Has ATPase activity.	0.977